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1h4i

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Revision as of 02:20, 12 September 2015

METHYLOBACTERIUM EXTORQUENS METHANOL DEHYDROGENASE

Structural highlights

1h4i is a 4 chain structure with sequence from Methylobacterium extorquens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Related:	1h4j
Activity:	Oxidoreductase, with EC number and 1.1.2.8 1.1.2.7 and 1.1.2.8
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum

Function

[DHM1_METEA] Catalyzes the oxidation of primary alcohols including methanol. [DHM2_METEA] Catalyzes the oxidation of primary alcohols including methanol.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

BACKGROUND: Methanol dehydrogenase (MDH) is a bacterial periplasmic quinoprotein; it has pyrrolo-quinoline quinone (PQQ) as its prosthetic group, requires Ca2+ for activity and uses cytochrome cL as its electron acceptor. Low-resolution structures of MDH have already been determined. RESULTS: The structure of the alpha 2 beta 2 tetramer of MDH from Methylobacterium extorquens has now been determined at 1.94 A with an R-factor of 19.85%. CONCLUSIONS: The alpha-subunit of MDH has an eight-fold radial symmetry, with its eight beta-sheets stabilized by a novel tryptophan docking motif. The PQQ in the active site is held in place by a coplanar tryptophan and by a novel disulphide ring formed between adjacent cysteines which are bonded by an unusual non-planar trans peptide bond. One of the carbonyl oxygens of PQQ is bonded to the Ca2+, probably facilitating attack on the substrate, and the other carbonyl oxygen is out of the plane of the ring, confirming the presence of the predicted free-radical semiquinone form of the prosthetic group.

The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A.,Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C Structure. 1995 Feb 15;3(2):177-87. PMID:7735834^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Ghosh M, Anthony C, Harlos K, Goodwin MG, Blake C. The refined structure of the quinoprotein methanol dehydrogenase from Methylobacterium extorquens at 1.94 A. Structure. 1995 Feb 15;3(2):177-87. PMID:7735834

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 See Also
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1h4i"

@@ Line 5: / Line 5: @@
 </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=PQQ:PYRROLOQUINOLINE+QUINONE'>PQQ</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1h4j|1h4j]]</td></tr>
-<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Alcohol_dehydrogenase_(acceptor) Alcohol dehydrogenase (acceptor)], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.99.8 1.1.99.8] </span></td></tr>
+<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Oxidoreductase Oxidoreductase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.1.2.7 and 1.1.2.8 1.1.2.7 and 1.1.2.8] </span></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4i OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1h4i RCSB], [http://www.ebi.ac.uk/pdbsum/1h4i PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1h4i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1h4i OCA], [http://pdbe.org/1h4i PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1h4i RCSB], [http://www.ebi.ac.uk/pdbsum/1h4i PDBsum]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/DHM1_METEX DHM1_METEX]] Catalyzes the oxidation of primary alcohols including methanol. [[http://www.uniprot.org/uniprot/DHM2_METEX DHM2_METEX]] Catalyzes the oxidation of primary alcohols including methanol.
+[[http://www.uniprot.org/uniprot/DHM1_METEA DHM1_METEA]] Catalyzes the oxidation of primary alcohols including methanol. [[http://www.uniprot.org/uniprot/DHM2_METEA DHM2_METEA]] Catalyzes the oxidation of primary alcohols including methanol.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 28: / Line 28: @@
 From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 </div>
+<div class="pdbe-citations 1h4i" style="background-color:#fffaf0;"></div>
 ==See Also==
@@ Line 36: / Line 37: @@
 </StructureSection>
 [[Category: Methylobacterium extorquens]]
+[[Category: Oxidoreductase]]
 [[Category: Anthony, C]]
 [[Category: Blake, C]]

1h4i

From Proteopedia

Revision as of 02:20, 12 September 2015

METHYLOBACTERIUM EXTORQUENS METHANOL DEHYDROGENASE

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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